G3CK85 · G3CK85_9ADEN

Function

function

Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.

Miscellaneous

All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.

Catalytic activity

  • Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|-Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).
    EC:3.4.22.39 (UniProtKB | ENZYME | Rhea)

Activity regulation

Requires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site52-53Cleavage; by autolysis
Active site55
Active site72
Active site123

GO annotations

AspectTerm
Cellular Componenthost cell nucleus
Cellular Componentvirion component
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionDNA binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Protease
  • EC number
  • Alternative names
    • Adenain
    • Adenovirus protease
      (AVP
      )
    • Adenovirus proteinase
    • Endoprotease

Gene names

    • Name
      L3

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Human/CAN/SW/2009/60[P60H20F60]
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus

Accessions

  • Primary accession
    G3CK85

Proteomes

Subcellular Location

Virion
Host nucleus
Note: Present in about 10 copies per virion.

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond105Interchain (with C-10 in cleaved protease cofactor pVI-C)

Keywords

Expression

Induction

Expressed in the late phase of the viral replicative cycle.

Keywords

Interaction

Subunit

Interacts with protease cofactor pVI-C; this interaction is necessary for protease activation.

Family & Domains

Sequence similarities

Belongs to the peptidase C5 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    209
  • Mass (Da)
    23,628
  • Last updated
    2011-11-16 v1
  • Checksum
    9B56C039B1F48D1F
MSGSSERELAAIVRDLGCGPYFLGTHDKRFPGFLAGDKLACAIVNTAGRETGGVHWLAFGWNPRSRTCYMFDPFGFSDRRLKQIYSFEYEAMLRRSALASSPDRCLSLEQSTQTVQGPDSAACGLFCCMFLHAFVHWPDRPMDGNPTMNLLTGVPNGMLQSPQVLPTLRRNQEELYRFLARHSHYFRSHRAAIEHATAFDKMKQLRVSQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HQ007053
EMBL· GenBank· DDBJ
AEK87027.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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